Abstract
TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron–sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron–sulfur cluster for catalyzing a non-redox reaction.
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